Fig. 3
From: Mapping the deformability of natural and designed cellulosomes in solution
Experimental scattering of the scaffoldin proteins ScaA, ScaH and ScaK and their analyses using ab initio envelope calculations. a Experimental scattering curve (orange points) of ScaA fitted by DAMMIN (black line) [73]; b ScaA; representation of 5 examples out of 10 fitted DAMMIN envelopes (colored red, cyan, blue, magenta and yellow); the overall mean normalized spatial discrepancy (NSD) calculated with DAMAVER for the 10 independent envelopes is 0.84 with a variation of 0.08, a value that indicates conservation of the shapes. All envelopes show similar kinks, indicating and coherent with the modular composition of the scaffoldin. c. Experimental scattering curve (light blue points) of ScaH fitted by DAMMIN (black line) [73]. d ScaH; representation of 5 examples out of 10 fitted DAMMIN envelopes (colored magenta, blue, yellow, cyan and green); the overall mean NSD calculated with DAMAVER for the 10 independent envelopes is 0.72 with a variation of 0.01, a value that indicates conservation of the shapes. The various envelopes highlight the modular composition of the scaffoldin, but locating individual modules within the shape is not possible. e ScaK; Experimental scattering curve of ScaK (green points) fitted by DAMMIN (black line) [73]. f ScaK; representation of 5 examples out of 10 fitted DAMMIN envelopes (colored blue, red, green, yellow and magenta); the overall mean NSD calculated with DAMAVER for the 10 independent envelopes is 0.73 with a variation of 0.02, a value that indicates conservation of the shapes. In coherence with Rg and Dmax values and the Kratky plot of scattering originating from ScaK, the envelopes show a more compact shape of this scaffoldin